Human NOV/CCN3 Biotinylated Antibody

NOV, also called CCN3, is one of six CCN (CYR61/CTGF/NOV) secreted proteins which share a common multimodular organization (1-4). NOV/CCN3 contains an N‑terminal IGFBP domain that appears to be non-functional and a vWF type C and thrombospondin type I domain which mediate oligomerization and matrix interactions, respectively (1, 2). The C-terminal cysteine knot domain interacts with several partners, including the matrix protein fibulin 1C (5), Notch-1 (6), and CCN2, with which it may heterodimerize (2). NOV/CCN3 also interacts with the gap junction protein Connexin43 and mediates suppression of proliferation (7). It also binds the calcium binding protein S100A4 and promotes calcium channel activation (8). The 357 amino acid (aa), 44 kDa human NOV/CCN3 shares 80% aa identity with mouse, rat and dog NOV/CCN3, and 78% aa identity with cow NOV/CCN3. NOV/CCN3 also shows 38-50% aa identity with other family members including WISP proteins, except for WISP-2/CCN5 which lacks the cysteine knot (1). NOV/CCN3 is widely expressed developmentally, especially in muscle, endothelium, nervous system, adrenal cortex and chondrocytes (1-4). In transformed cells, a 32 kDa N-terminally truncated form lacks the signal sequence is localized to the nucleus. Truncation allows a C‑terminal nuclear localization sequence to be active (9). Nuclear NOV/CCN3 acts as a transcriptional repressor but promotes proliferation, presumably by interfering with growth control (9). Full length NOV/CCN3 is a secreted matricellular protein which inhibits cell growth. Interaction of NOV/CCN3 with integrins alpha_v beta₃ and  alpha₅ beta₁ mediates endothelial cell adhesion, chemotaxis, and promotes angiogenesis (10, 11). Over-expression of NOV/CCN3 downregulates myogenic genes such as MyoD (12).